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dc.rights.licenseopenen_US
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorREDDY, Post Sai
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorD'ESTAINTOT, Beatrice Langlois
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGRANIER, Thierry
hal.structure.identifierARN : régulations naturelle et artificielle
dc.contributor.authorMACKERETH, Cameron D.
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorFISCHER DUROLA, Lucile
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHUC, Ivan
dc.date.accessioned2020-05-11T09:40:42Z
dc.date.available2020-05-11T09:40:42Z
dc.date.issued2019
dc.identifier.issn0947-6539en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/7511
dc.description.abstractEnThe development of large synthetic ligands could be useful to target the sizeable surface areas involved in protein-protein interactions. Herein, we present long helical aromatic oligoamide foldamers bearing proteinogenic side chains that cover up to 450 angstrom(2) of the human carbonic anhydrase II (HCA) surface. The foldamers are composed of aminoquinolinecarboxylic acids bearing proteinogenic side chains and of more flexible aminomethyl-pyridinecarboxylic acids that enhance helix handedness dynamics. Crystal structures of HCA-foldamer complexes were obtained with a 9- and a 14-mer both showing extensive protein-foldamer hydrophobic contacts. In addition, foldamer-foldamer interactions seem to be prevalent in the crystal packing, leading to the peculiar formation of an HCA superhelix wound around a rod of stacked foldamers. Solution studies confirm the positioning of the foldamer at the protein surface as well as a dimerization of the complexes.
dc.language.isoENen_US
dc.subject.enaromatic oligoamides
dc.subject.enfoldamers
dc.subject.enprotein surface recognition
dc.subject.enstructure elucidation
dc.subject.enX-ray crystallography
dc.title.enStructure Elucidation of Helical Aromatic Foldamer-Protein Complexes with Large Contact Surface Areas
dc.typeArticle de revueen_US
dc.identifier.doi10.1002/chem.201902942
dc.subject.halChimie/Matériauxen_US
bordeaux.journalChemistry-a European Journalen_US
bordeaux.page11042-11047en_US
bordeaux.volume25en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03182130
hal.version1
hal.date.transferred2021-03-26T09:45:05Z
hal.exporttrue
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